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节肢动物交叉反应性的分子基础:虾、屋尘螨和蟑螂原肌球蛋白的IgE结合交叉反应表位

Molecular basis of arthropod cross-reactivity: IgE-binding cross-reactive epitopes of shrimp, house dust mite and cockroach tropomyosins.

作者信息

Ayuso Rosalia, Reese Gerald, Leong-Kee Susan, Plante Matthew, Lehrer Samuel B

机构信息

Section of Allergy and Clinical Immunology, Tulane University School of Medicine, 1700 Perdido Street, New Orleans, LA 70112, USA.

出版信息

Int Arch Allergy Immunol. 2002 Sep;129(1):38-48. doi: 10.1159/000065172.

Abstract

BACKGROUND

Shrimp may cross-react with other crustaceans and mollusks and nonedible arthropods such as insects (cockroach and chironomids), arachnids (house dust mites) and even nematodes. Since the muscle protein tropomyosin has been implicated as a possible cross-reacting allergen, this study characterized the IgE-binding epitopes in shrimp tropomyosin, Pen a 1, that cross-react with other allergenic invertebrate tropomyosins in house dust mites (Der p 10, Der f 10) and cockroaches (Per a 7). Pen a 1-reactive sera from shrimp-allergic subjects were used to evaluate the effect on IgE binding of different amino acid substitutions in Pen a 1 epitopes based on homologous sequences in Per a 7 and Der p 10/Der f 10.

METHODS

Peptides were synthesized spanning the length of Pen a 1 IgE-binding epitopes and amino acid substitutions were performed based on homologous amino acid sequences from Per a 7 and Der p 10/Der f 10.

RESULTS

7/8 individually recognized Pen a 1 epitopes (2, 3a, 3b, 4, 5a, 5b and 5c) had an identical amino acid sequence with lobster allergen, Hom a 1, 4/8 (3a, 3b, 4 and 5a) with Der p 10 and Der f 10, and 5/8 (2, 3a, 3b, 4 and 5a) with Per a 7. In addition, even homologous regions of other arthropod tropomyosins that differ in one or more amino acids from the sequences of Pen a 1 epitopes are still recognized by shrimp-allergic IgE antibodies. In total, shrimp-allergic sera recognize 6/8 peptides homologous to Pen a 1 epitopes in Per a 7, 7/8 in Der p 10/Der f 10, and 7/8 epitopes in Hom a 1.

CONCLUSIONS

The IgE recognition by shrimp-allergic individuals of identified and/or similar amino acid sequences homologous to Pen a 1 epitopes in mite, cockroach and lobster tropomyosins are the basis of the in vitro cross-reactivity among invertebrate species. Based on amino acid sequence similarity and epitope reactivity, lobster tropomyosin has the strongest and cockroach the least cross-reactivity with shrimp. The clinical relevance of these cross-reactivities in developing allergic reactions to different arthropods needs to be determined.

摘要

背景

虾可能与其他甲壳类动物、软体动物以及不可食用的节肢动物如昆虫(蟑螂和摇蚊)、蛛形纲动物(屋尘螨)甚至线虫发生交叉反应。由于肌肉蛋白原肌球蛋白被认为是一种可能的交叉反应性变应原,本研究对虾原肌球蛋白Pen a 1中的IgE结合表位进行了表征,该表位与屋尘螨(Der p 10、Der f 10)和蟑螂(Per a 7)中其他变应性无脊椎动物原肌球蛋白发生交叉反应。来自对虾过敏受试者的Pen a 1反应性血清用于评估基于Per a 7和Der p 10/Der f 10中的同源序列,Pen a 1表位中不同氨基酸取代对IgE结合的影响。

方法

合成跨越Pen a 1 IgE结合表位长度的肽,并根据来自Per a 7和Der p 10/Der f 10的同源氨基酸序列进行氨基酸取代。

结果

8个单独识别的Pen a 1表位(2、3a、3b、4、5a、5b和5c)中有7个与龙虾变应原Hom a 1具有相同的氨基酸序列,8个中有4个(3a、3b、4和5a)与Der p 10和Der f 10相同,8个中有5个(2、3a、3b、4和5a)与Per a 7相同。此外,即使其他节肢动物原肌球蛋白的同源区域与Pen a 1表位序列在一个或多个氨基酸上不同,仍能被对虾过敏的IgE抗体识别。总体而言,对虾过敏的血清识别Per a 7中6/8个与Pen a 1表位同源的肽、Der p 10/Der f 10中7/8个以及Hom a 1中7/8个表位。

结论

对虾过敏个体对螨、蟑螂和龙虾原肌球蛋白中与Pen a 1表位同源的已鉴定和/或相似氨基酸序列的IgE识别是无脊椎动物物种间体外交叉反应性的基础。基于氨基酸序列相似性和表位反应性,龙虾原肌球蛋白与虾的交叉反应性最强,蟑螂最弱。这些交叉反应性在引发对不同节肢动物过敏反应中的临床相关性有待确定。

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